Distinct B subunits of PP2A regulate the NF‐κB signalling pathway through dephosphorylation of IKKβ, IκBα and RelA. Issue 24 (3rd December 2017)

• Record Type: Journal Article
• Authors: Tsuchiya, Yoshihiro; Osaki, Keiko; Kanamoto, Mayu; Nakao, Yuki; Takahashi, Ena; Higuchi, Toru; Kamata, Hideaki
• Is Part Of: FEBS letters. Volume 591:Issue 24(2017)
• Page Start: 4083
• Page End: 4094
• Publication Date: 2017-12-03
• Subjects: NF‐kappa B -- protein phosphatase -- protein phosphatase 2 A (PP2A); Biochemistry -- Periodicals; Biophysics -- Periodicals; Molecular biology -- Periodicals; Biochimie -- Périodiques; Biochemistry; Biophysics; Molecular biology; Periodicals; 572.05
• DOI: 10.1002/1873-3468.12912
• Languages: English
• ISSNs: 0014-5793

Abstract

Abstract : PP2A is composed of a scaffolding subunit (A), a catalytic subunit (C) and a regulatory subunit (B) that is classified into four families including B, B′, B′′ and B′′′/striatin. Here, we found that a distinct PP2A complex regulates NF‐κB signalling by dephosphorylation of IKKβ, IκBα and RelA/p65. The PP2A core enzyme AC dimer and the holoenzyme AB′′′C trimer dephosphorylate IKKβ, IκBα and RelA, whereas the ABC trimer dephosphorylates IκBα but not IKKβ and RelA in cells. In contrast, AB′C and AB′′C trimers have little effect on dephosphorylation of these signalling proteins. These results suggest that different forms of PP2A regulate NF‐κB pathway signalling through multiple steps each in a different manner, thereby finely tuning NF‐κB‐ and IKKβ‐mediated cellular responses. Abstract :